Q4QI30 · Q4QI30_LEIMA

  • Protein
    Endonuclease III homolog
  • Gene
    NTH1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular FunctionDNA binding
Molecular FunctionDNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Molecular Functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
Biological Processbase-excision repair, AP site formation
Biological Processnucleotide-excision repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endonuclease III homolog
  • EC number
  • Alternative names
    • Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase
      (DNA glycosylase/AP lyase
      )

Gene names

    • Name
      NTH1
    • ORF names
      LMJF_09_0050

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MHOM/IL/81/Friedlin
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    Q4QI30

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain58-208HhH-GPD
Region237-257Disordered

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    29,495
  • Last updated
    2005-07-19 v1
  • Checksum
    ACFBF8754A67EB2D
MNKRSFTPPSNWAQLFARLEDYRKHLKAPVDTMGCHRLRDETAPKEVQRFHTLVALMLSAQTKDVVTAAAMDTLIKRELTVQSVHAMTETELDKHICKVGFHNTKARNIKEVAAILMKNYDGKVPREYAELIALPGVGPKMANLFFQDADHRVIGIGVDTHVHRISQRYRWVPSTVKTPEDTRKALESWLPREHWGTINSLMVGLGQTVCTPLRPKCDICELSDICPNAFKERRQKRLRAKAPLMEKEEPVSHRKRR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR796405
EMBL· GenBank· DDBJ
CAJ02303.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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